CAZyme Information: MGYG000003335_01489

Basic Information

• Species: GCA-900066135 sp900543575
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; GCA-900066135; GCA-900066135 sp900543575
• CAZyme ID: MGYG000003335_01489
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
816	MGYG000003335_163|CGC2	94318.15	5.1844

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003335	3295822	MAG	China	Asia

• Gene Location: Start: 27378; End: 29828 Strand: -

Full Sequence      

MEKMWNVYLIHHSHTDIGYTERQEKIMRYHYDFIRQAIEILDDIHSGKTTGCDGFVWQCE
NHWQIENFYQMADEELQKKFEAYVRSGEIGLSGNYLNMTELVSAPVLNDSLDKMQAYGEK
TGHPIVAGMSADINGLAWGYADALYNHGVRYFYTALHPHHGMFPNYHKTLPYYWEGPSGN
RVLMWNGDHYHLGNEMFFSPHSGSAYTIRDELYDHINSKLFYDVEDEEAAEEAALHTRIE
RYLYNLEDEKYPYSMVPFMVSGAITDNAPPSKEIAHRVNKLNEYYKGKIHFQMATLEQFF
QEVEKQAKDIPVYRGDFTDWWADGIGSTPHPVKLYLDAERKYSLCEKMDPEGTRGSAELR
EKAREELMMYAEHTWGYSSSVSEPWDSMVGSLELKKDAYAINANTDISRNLDILMAQEGE
VSIRQDKPQRYVIINPHDEVLHTNAYIYIEFWEYIDGKPFDASRMDLVVRNTETGAIIPS
QLKQIARALQVELEVSMKPHEKFIAEITRKEKPYFTIQNYAHVGAEGVEDILQDSNNRLD
EDVIDTDDFHIETDGNGIKKIIWKKDGSDLIKEKGTAAFSGVYEITPMDGVSACEVRRRM
GRNRKSKGTIRSFCQLKNRKIVENGAVYCALELRYELKGTRLYDIFLKVYKHMPKIEATV
RIHKTSRWEPENLYISLPFTAGDGSEFYIDKTGCVIRPGIDQLPGTCQDFYLIQNGVAWT
SKEKTVSIITKDAPLISLGGLEAKRINLCNGKDTKRNQSEVYSWPMNNFWETNFKVDLGG
FYEFRYILDVEEGEEIHDTFRRCQAENEGILTGYTE

Enzyme Prediction     

No EC number prediction in MGYG000003335_01489.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd10791	GH38N_AMII_like_1	7.20e-73	7	283	2	254	N-terminal catalytic domain of mainly uncharacterized eukaryotic proteins similar to alpha-mannosidases; glycoside hydrolase family 38 (GH38). The subfamily of mainly uncharacterized eukaryotic proteins shows sequence homology with class II alpha-mannosidases (AlphaAMIIs). AlphaAMIIs possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyze the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. This subfamily belongs to the GH38 family of retaining glycosyl hydrolases, which employ a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst.
pfam01074	Glyco_hydro_38	1.18e-09	6	320	1	270	Glycosyl hydrolases family 38 N-terminal domain. Glycosyl hydrolases are key enzymes of carbohydrate metabolism.
cd10786	GH38N_AMII_like	7.81e-07	6	196	1	185	N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38). Alpha-mannosidases (EC 3.2.1.24) are extensively found in eukaryotes and play important roles in the processing of newly formed N-glycans and in degradation of mature glycoproteins. A deficiency of this enzyme causes the lysosomal storage disease alpha-mannosidosis. Many bacterial and archaeal species also possess putative alpha-mannosidases, but their activity and specificity is largely unknown. Based on different functional characteristics and sequence homology, alpha-mannosidases have been organized into two classes (class I, belonging to glycoside hydrolase family 47, and class II, belonging to glycoside hydrolase family 38). Members of this family corresponds to class II alpha-mannosidases (alphaMII), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst.
PRK09819	PRK09819	5.68e-06	266	319	221	273	mannosylglycerate hydrolase.
cd10815	GH38N_AMII_EcMngB_like	1.62e-05	266	319	216	268	N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial homologs; glycoside hydrolase family 38 (GH38). The bacterial subfamily is represented by Escherichia coli alpha-mannosidase MngB, which is encoded by the mngB gene (previously called ybgG). MngB exhibits alpha-mannosidase activity that converts 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. A divalent metal ion is required for its activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SET75050.1	0.0	1	816	3	820
AUS96542.1	1.04e-314	1	814	14	829
ANS75706.1	1.47e-314	1	814	3	819
QDA73873.1	3.25e-249	1	814	3	808
SQI58910.1	4.54e-249	1	811	1	807

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000059	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003335_01489.